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. Author manuscript; available in PMC: 2011 Apr 15.
Published in final edited form as: J Phys Chem B. 2010 Apr 15;114(14):4755–4762. doi: 10.1021/jp911533q

Fig. 5.

Fig. 5

(a) Thermal distributions of the fractions of helix <H(i)> and β-strand <S(i)> structure formed by the residues i in Aβ10–40 peptides bound to the fibril: the MT (filled circles), the WT (open circles). (b) Distributions <H(i)> and <S(i)> computed for Aβ10–40 dimer: the MT (filled circles), the WT (open circles). The deletion of backbone HBs in the MT induces strand-to-helix structural conversion in the dimers and incoming peptides. The distributions <H(i)> and <S(i)> are obtained at 360K.